KpATCC43816 Protein target profile

phosphoenolpyruvate-protein phosphotransferase

Accession: VK055_4287

Gene: AIK82832.1 ptsP 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3H2B7

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Length 748

Pocket druggability (P2Rank · AlphaFold DB model) 0.848

Metabolic reactions 3

Chokepoint Yes

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 9 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 90.2% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 2.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 35.852 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 86.54 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.848

Structure A0A0H3H2B7

Pocket Pocket 1

Druggability (FPocket) 0.428

Structure A0A0H3H2B7

Pocket Pocket 28

ColabFold model

P2Rank 0.894 · Pocket 1

FPocket 0.851 · Pocket 8

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 108 / 4744 genomes with a hit

Prevalence 2.3%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction, no isoenzyme backup detected, more central than 90.2% of genes in this genome, no human homolog detected.

Relative network centrality 90.2% more central than 90.2% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLTRLREIVEKVASAPRLNEALDILVTDVCQAMETEVCSVYLADNDRRCYYLMATRGLKKPRGRTVALAFDEGLVGLVGRLAEPINLADAQKHPSFKYIPAVKEDRFRAFLGVPIIQRRQLLGVLVVQQRELRQFDESEESFLVTLATQMAAILSQSQLNALFGQYRQTRIRALPASSGVAIAEGWMDVSLPLMEQVYEASTLDTASERERLTGALEEAANEFRRYSKRYAAGAQKETAAIFDLYSHLLSDARLRRELFAEVDKGAVAEWAVKKIIEKFAEQFAALSDGYLKERAGDLRTLGQRLLFHLDDSIQGPNTWPARIILVADELSATTLAEVPQDRLAGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSLLHGHTLIVDGYRGELLVDPEPVLLQEYQRLISEENELSRLAEDDLQRASELKSGERVKVMLNAGLSPEHEEKLGSFVDGIGLYRTEIPFMLQSGFPSEEEQVAQYQGMLQMFNSKPVTLRTLDIGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLSILLPMVTSLEEVDEARRLIDRASREVEEMIGYAIPRPRLGVMLEVPSMVFMLPQLASRIDFISVGTNDLTQYLLAVDRNNTRVASMYDSLHPAVLRALAMIAHDAERFGIDLRLCGEMAGDPMCVTILIGLGYRHLSMNGRSVARVKYLLRRIDIEEAQELSRRSLDAQMTAEVRHQVAAFMERRGLGGLIRGGR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.7.3.9

Gene Ontology (GO)

GO:0016772 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0005515 Binding to a protein.
GO:0009401 The uptake and phosphorylation of specific carbohydrates from the extracellular environment; uptake and phosphorylation are coupled, making the PTS a link between the uptake and metabolism of sugars; phosphoenolpyruvate is the original phosphate donor; phosphoenolpyruvate passes the phosphate via a signal transduction pathway, to enzyme 1 (E1), which in turn passes it on to the histidine protein, HPr; the next step in the system involves sugar-specific membrane-bound complex, enzyme 2 (EII), which transports the sugar into the cell; it includes the sugar permease, which catalyzes the transport reactions; EII is usually divided into three different domains, EIIA, EIIB, and EIIC.
GO:0016310 The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
GO:0046872 Binding to a metal ion.
GO:0008965 Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

42 records

Show feature table

Start	End	DB	Term	Name
175	403	Gene3D	G3DSA:3.50.30.10	Phosphohistidine domain
307	403	FunFam	G3DSA:3.50.30.10:FF:000003	Phosphoenolpyruvate-protein phosphotransferase ptsP
351	362	ProSitePatterns	PS00370	PEP-utilizing enzymes phosphorylation site signature.
351	362	InterPro	IPR018274	PEP-utilising enzyme, active site
666	678	PRINTS	PR01736	Phosphoenolpyruvate-protein phosphotransferase signature
613	628	PRINTS	PR01736	Phosphoenolpyruvate-protein phosphotransferase signature
459	478	PRINTS	PR01736	Phosphoenolpyruvate-protein phosphotransferase signature
630	645	PRINTS	PR01736	Phosphoenolpyruvate-protein phosphotransferase signature
1	163	Gene3D	G3DSA:3.30.450.40	-
1	163	InterPro	IPR029016	GAF-like domain superfamily
209	229	Coils	Coil	Coil
1	162	FunFam	G3DSA:3.30.450.40:FF:000012	Phosphoenolpyruvate-protein phosphotransferase PtsP
190	313	Gene3D	G3DSA:1.10.274.10	-
190	313	InterPro	IPR036618	PtsI, HPr-binding domain superfamily
82	738	PANTHER	PTHR46244	PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE
558	578	Coils	Coil	Coil
425	714	SUPERFAMILY	SSF51621	Phosphoenolpyruvate/pyruvate domain
425	714	InterPro	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
293	412	SUPERFAMILY	SSF52009	Phosphohistidine domain
293	412	InterPro	IPR036637	Phosphohistidine domain superfamily
404	736	Gene3D	G3DSA:3.20.20.60	-
404	736	InterPro	IPR040442	Pyruvate kinase-like domain superfamily
198	309	SUPERFAMILY	SSF47831	Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain
198	309	InterPro	IPR036618	PtsI, HPr-binding domain superfamily
18	152	Pfam	PF01590	GAF domain
18	152	InterPro	IPR003018	GAF domain
174	294	Pfam	PF05524	PEP-utilising enzyme, N-terminal
174	294	InterPro	IPR008731	Phosphotransferase system, enzyme I N-terminal
321	391	Pfam	PF00391	PEP-utilising enzyme, mobile domain
321	391	InterPro	IPR008279	PEP-utilising enzyme, mobile domain
190	313	FunFam	G3DSA:1.10.274.10:FF:000002	Phosphoenolpyruvate-protein phosphotransferase PtsP
2	159	SUPERFAMILY	SSF55781	GAF domain-like
425	707	Pfam	PF02896	PEP-utilising enzyme, PEP-binding domain
425	707	InterPro	IPR000121	PEP-utilising enzyme, C-terminal
17	164	SMART	SM00065	gaf_1
17	164	InterPro	IPR003018	GAF domain
404	736	FunFam	G3DSA:3.20.20.60:FF:000012	Phosphoenolpyruvate-protein phosphotransferase PtsP
175	729	NCBIfam	TIGR01417	phosphoenolpyruvate--protein phosphotransferase
175	729	InterPro	IPR006318	Phosphotransferase system, enzyme I-like
402	422	Coils	Coil	Coil
613	631	ProSitePatterns	PS00742	PEP-utilizing enzymes signature 2.
613	631	InterPro	IPR023151	PEP-utilising enzyme, conserved site

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.848

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Surrounding area

Pocket 2 P2Rank #2

0.435

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Surrounding area

Pocket 3 P2Rank #3

0.298

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Surrounding area

Pocket 4 P2Rank #4

0.154

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Surrounding area

Pocket 5 P2Rank #5

0.112

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #28

0.428

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.894

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Surrounding area

Pocket 2 P2Rank #2

0.601

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Surrounding area

Pocket 3 P2Rank #3

0.566

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Surrounding area

Pocket 4 P2Rank #4

0.318

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Surrounding area

Pocket 5 P2Rank #5

0.219

Likely same site as FPocket 8 7.0 Å 9 shared residues 53% of smaller site

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #8

0.851 Unusual size

Likely same site as P2Rank 5 7.0 Å 9 shared residues 53% of smaller site

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Surrounding area

Pocket 2 FPocket #22

0.27

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3H2B7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4287	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

55 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

6NQ PDB via homolog 569.1 Da · LogP -0.65 · TPSA 261.7 Open detail RCSB PDB

OXL PDB via homolog Detail RCSB PDB

P4G PDB via homolog Detail RCSB PDB

PEP PDB via homolog Detail RCSB PDB

PO3 PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
6NQ RCSB PDB	5JVL	P22221	569.1 Da LogP -0.65 TPSA 261.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
OXL RCSB PDB	2HWG	P08839	88.0 Da LogP -3.51 TPSA 80.3	✓ Ro5	✓ Clean	`C(=O)(C(=O)[O-])[O-]`
P4G RCSB PDB	3CI6	Q6FEW8	162.2 Da LogP 1.08 TPSA 27.7	✓ Ro5	✓ Clean	`CCOCCOCCOCC`
PEP RCSB PDB	5JVL	P22221	168.0 Da LogP -0.31 TPSA 104.1	✓ Ro5	✓ Clean	`C=C(C(=O)O)OP(=O)(O)O`
PO3 RCSB PDB	2MP0	P08839	79.0 Da LogP -1.64 TPSA 63.2	✓ Ro5	✓ Clean	`[O-][P-](=O)[O-]`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC5859031 ZINC	1.000	294.4 Da LogP 1.13 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCC`
ZINC4974293 ZINC	0.786	280.4 Da LogP 1.08 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCOCCOCCOCC`
ZINC12360002 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.703	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC5650743 ZINC	0.688	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	0.688	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC16688007 ZINC	0.647	446.8 Da LogP 4.03 TPSA 36.9	✓ Ro5	✓ Clean	`CCOCCOCCSCCSCCSCCSCCOCCOCC`
ZINC13518964 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.641	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC12503850 ZINC	0.632	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.632	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.632	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.632	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC4096224 ZINC	0.631	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC105469665 ZINC	0.627	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.627	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.627	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.627	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.627	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.627	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.627	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC105372833 ZINC	0.615	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.615	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.615	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.615	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.614	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC2173592 ZINC	0.600	216.4 Da LogP 3.79 TPSA 18.5	✓ Ro5	✓ Clean	`CCOCCCCCCCCCOCC`
ZINC28278447 ZINC	0.600	230.4 Da LogP 4.18 TPSA 18.5	✓ Ro5	✓ Clean	`CCOCCCCCCCCCCOCC`
ZINC3871401 ZINC	0.594	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC4096223 ZINC	0.594	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3H2B7

Pathways

KEGG R02628 BioCyc 2.7.3.9-RXN BioCyc RXN-17355 BioCyc RXN-17354